NR1H2_BOVIN
ID NR1H2_BOVIN Reviewed; 455 AA.
AC Q5BIS6; Q32KU5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Oxysterols receptor LXR-beta;
DE AltName: Full=Liver X receptor beta;
DE AltName: Full=Nuclear receptor subfamily 1 group H member 2;
GN Name=NR1H2; Synonyms=LXRB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Nuclear receptor that exhibits a ligand-dependent
CC transcriptional activation activity (By similarity). Binds
CC preferentially to double-stranded oligonucleotide direct repeats having
CC the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4).
CC Regulates cholesterol uptake through MYLIP-dependent ubiquitination of
CC LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA
CC for the regulation of genes involved in liver metabolism (By
CC similarity). Induces LPCAT3-dependent phospholipid remodeling in
CC endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1
CC processing and lipogenesis (By similarity). Via LPCAT3, triggers the
CC incorporation of arachidonate into phosphatidylcholines of ER
CC membranes, increasing membrane dynamics and enabling triacylglycerols
CC transfer to nascent very low-density lipoprotein (VLDL) particles. Via
CC LPCAT3 also counteracts lipid-induced ER stress response and
CC inflammation, likely by modulating SRC kinase membrane
CC compartmentalization and limiting the synthesis of lipid inflammatory
CC mediators (By similarity). Plays an anti-inflammatory role during the
CC hepatic acute phase response by acting as a corepressor: inhibits the
CC hepatic acute phase response by preventing dissociation of the N-Cor
CC corepressor complex (By similarity). {ECO:0000250|UniProtKB:P55055,
CC ECO:0000250|UniProtKB:Q60644}.
CC -!- SUBUNIT: Forms a heterodimer with RXR. Interacts with CCAR2 (via N-
CC terminus) in a ligand-independent manner. Interacts (when sumoylated)
CC with GPS2; interaction with GPS2 onto hepatic acute phase protein
CC promoters prevents N-Cor corepressor complex dissociation (By
CC similarity). Interacts with ABCA12 and ABCA1; this interaction is
CC required for ABCA1 localization to the cell surface and is necessary
CC for its normal activity and stability (By similarity).
CC {ECO:0000250|UniProtKB:P55055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- PTM: Sumoylated by SUMO2 at Lys-404 and Lys-442 during the hepatic
CC acute phase response, leading to promote interaction with GPS2 and
CC prevent N-Cor corepressor complex dissociation.
CC {ECO:0000250|UniProtKB:P55055}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT021148; AAX31330.1; -; mRNA.
DR EMBL; BC109925; AAI09926.1; -; mRNA.
DR RefSeq; XP_005219286.1; XM_005219229.3.
DR AlphaFoldDB; Q5BIS6; -.
DR SMR; Q5BIS6; -.
DR STRING; 9913.ENSBTAP00000004229; -.
DR PaxDb; Q5BIS6; -.
DR Ensembl; ENSBTAT00000004229; ENSBTAP00000004229; ENSBTAG00000003264.
DR GeneID; 509622; -.
DR CTD; 7376; -.
DR VEuPathDB; HostDB:ENSBTAG00000003264; -.
DR VGNC; VGNC:32230; NR1H2.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161465; -.
DR InParanoid; Q5BIS6; -.
DR OMA; GMREQCE; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000003264; Expressed in adenohypophysis and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0032369; P:negative regulation of lipid transport; IEA:Ensembl.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IEA:Ensembl.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0090108; P:positive regulation of high-density lipoprotein particle assembly; IEA:Ensembl.
DR GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0090187; P:positive regulation of pancreatic juice secretion; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0090340; P:positive regulation of secretion of lysosomal enzymes; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR023257; Liver_X_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR02034; LIVERXRECPTR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..455
FT /note="Oxysterols receptor LXR-beta"
FT /id="PRO_0000053531"
FT DOMAIN 217..455
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 79..156
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 82..102
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 120..144
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..80
FT /note="Transactivation AF-1; required for ligand-
FT independent transactivation function"
FT /evidence="ECO:0000250|UniProtKB:P55055"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..455
FT /note="Transactivation AF-2; required for ligand-dependent
FT transactivation function; mediates interaction with CCAR2"
FT /evidence="ECO:0000250|UniProtKB:P55055"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55055"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55055"
SQ SEQUENCE 455 AA; 49988 MW; BAAC2E03C31FF7AC CRC64;
MSTPTTNSVD TPLPGNGPST PSSSPGGKED GPEPCPGGAD PDVPSTDGAD SASVVVILDT
AEEPERKRKK GPAPKMLGDE LCQVCGDTAS GFHYNVLSCE GCKGFFRRSV IRGGAGRYAC
RGGGTCQMDA FMRRKCQQCR LRKCKEAGMR EQCVLSKEQI RKKKIRKQQQ QQQQQSSPTG
PGVSSSSPAS GPGASPGGSD GGGQGSGEGE GVQLTAAQEL MIQQLVAAQL QCNKRSFSDQ
PKVTPWPLGA DPQSRDARQQ RFAHFTELAI ISVQEIVDFA KQVPGFLQLG REDQIALLKA
STIEIMLLET ARRYNHETEC ITFLKDFTYS KDDFHRAGLQ VEFINPIFEF SRAMRRLGLD
DAEYALLIAI NIFSADRPNV QEPSRVEALQ QPYVDALLSY TRIKRPQDQL RFPRMLMKLV
SLRTLSSVHS EQVFALRLQD KKLPPLLSEI WDVHE
